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Journal ArticleDOI

The major birch pollen allergen, Bet v 1, shows ribonuclease activity

Albrecht Bufe, +4 more
- 01 Jan 1996 - 
- Vol. 199, Iss: 3, pp 413-415
TLDR
Purified recombinant Bet v 1 was shown to degrade plant RNA and the monomer and the dimer of Bet v1 showed RNase activity.
Abstract
The major birch (Betula alba L.) pollen allergen, Bet v 1, has been shown to be homologous to pathogenesis-related proteins in a number of plants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley and to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was separated in an RNase activity gel. Four major RNase bands were excised from the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by Western blotting with a specific Bet v 1 monoclonal antibody and patient's serum. Thus the monomer and the dimer of Bet v 1 showed RNase activity. Purified recombinant Bet v 1 was shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units · mg−1.

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Citations
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Journal ArticleDOI

Allergic Rhinitis and Its Impact on Asthma

TL;DR: This systematic review and meta-analyses confirmed the findings of a previous study published in “Rhinitis and Asthma: Causes and Prevention, 2nd Ed.” (2015) as well as new findings of “Mechanisms of Respiratory Disease and Allergology,” which confirmed the role of EMTs in the development of these diseases.
Journal ArticleDOI

Significance of Inducible Defense-related Proteins in Infected Plants

TL;DR: The evolutionary conservation of similar defense-related proteins in monocots and dicots, but also their divergent occurrence in other conditions, suggest that these proteins serve essential functions in plant life, whether in defense or not.
Journal ArticleDOI

The roles of segmental and tandem gene duplication in the evolution of large gene families in Arabidopsis thaliana

TL;DR: Combining information about genomic segmental duplications, gene family phylogenies, and gene positions provides a method to evaluate contributions of tandem duplication and segmental genome duplication in the generation and maintenance of gene families.
Journal ArticleDOI

Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes

TL;DR: A comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems in prokaryotes is reported, and indications that the two-gene module that encodes a minimal nucleotidyl transferase and the accompanying HEPN protein, and is extremely abundant in many archaea and bacteria might comprise a novel TAS are presented.
Journal ArticleDOI

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy.

TL;DR: The three-dimensional structure of the major birch pollen allergen, the 17,500 Mr acidic protein Bet v 1 (from the birch, Betula verrucosa), is presented as determined both in the crystalline state by X-ray diffraction and in solution by NMR spectroscopy.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene.

TL;DR: The complete nucleotide sequence and deduced amino acid sequence of a cDNA clone coding for the major pollen allergen (BetvI) of white birch shows 55% sequence identity with a pea disease resistance response gene, indicating that BetvI may be involved in pathogen resistance of pollen.
Journal ArticleDOI

Gene structure and in situ transcript localization of pathogenesis-related protein 1 in parsley.

TL;DR: Three nearly full-length cDNAs complementary to mRNAs encoding two PR1 proteins in parsley demonstrated rapid and massive PR1 mRNA accumulation around infection sites.
Journal ArticleDOI

High sequence similarity between a ribonuclease from ginseng calluses and fungus-elicited proteins from parsley indicates that intracellular pathogenesis-related proteins are ribonucleases

TL;DR: There was 60–70% sequence identity with two intracellular pathogenesis-related (IPR) proteins from parsley, indicating that not only these two proteins, but also homologous IPR proteins identified in other plant species are ribonucleases.
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